3H63
Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms originally soaked with cantharidin (which is present in the structure in the hydrolyzed form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-25 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.98340 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 154.464, 41.784, 105.833 |
| Unit cell angles | 90.00, 96.88, 90.00 |
Refinement procedure
| Resolution | 38.350 - 1.300 |
| R-factor | 0.16409 |
| Rwork | 0.161 |
| R-free | 0.19108 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1s95 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.371 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.4.0067) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.370 |
| High resolution limit [Å] | 1.300 | 1.300 |
| Rmerge | 0.060 | 0.380 |
| Number of reflections | 164908 | |
| <I/σ(I)> | 16.9 | 2.8 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6.3 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 289 | 10mM Tris-HCl, 40% MPD, 20% PEG MME 5000, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
